6E1C

Crystal structure of a MauG-like protein associated with microbial copper homeostasis

6E1C の概要

• エントリーDOI: 10.2210/pdb6e1c/pdb
• 分子名称: Di-heme enzyme, HEME C, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: di-heme cytochrome c peroxidase., metal binding protein
• 由来する生物種: Methylosinus trichosporium OB3b
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 87998.03

構造登録者

Dassama, L.M.K.,Rosenzweig, A.C. (登録日: 2018-07-09, 公開日: 2019-07-17, 最終更新日: 2024-12-25)

主引用文献

Kenney, G.E.,Dassama, L.M.K.,Manesis, A.C.,Ross, M.O.,Chen, S.,Hoffman, B.M.,Rosenzweig, A.C.
MbnH is a diheme MauG-like protein associated with microbial copper homeostasis.
J.Biol.Chem., 294:16141-16151, 2019

PubMed Abstract: Methanobactins (Mbns) are ribosomally-produced, post-translationally modified peptidic copper-binding natural products produced under conditions of copper limitation. Genes encoding Mbn biosynthetic and transport proteins have been identified in a wide variety of bacteria, indicating a broader role for Mbns in bacterial metal homeostasis. Many of the genes in the Mbn operons have been assigned functions, but two genes usually present, and , encode uncharacterized proteins predicted to reside in the periplasm. MbnH belongs to the bacterial diheme cytochrome peroxidase (bCcP)/MauG protein family, and MbnP contains no domains of known function. Here, we performed a detailed bioinformatic analysis of both proteins and have biochemically characterized MbnH from () OB3b. We note that the and genes typically co-occur and are located proximal to genes associated with microbial copper homeostasis. Our bioinformatics analysis also revealed that the bCcP/MauG family is significantly more diverse than originally appreciated, and that MbnH is most closely related to the MauG subfamily. A 2.6 Å resolution structure of OB3b MbnH combined with spectroscopic data and peroxidase activity assays provided evidence that MbnH indeed more closely resembles MauG than bCcPs, although its redox properties are significantly different from those of MauG. The overall similarity of MbnH to MauG suggests that MbnH could post-translationally modify a macromolecule, such as internalized CuMbn or its uncharacterized partner protein, MbnP. Our results indicate that MbnH is a MauG-like diheme protein that is likely involved in microbial copper homeostasis and represents a new family within the bCcP/MauG superfamily.

PubMed: 31511324
DOI: 10.1074/jbc.RA119.010202

実験手法

X-RAY DIFFRACTION (2.617 Å)